title: Protein components of a cytochrome P-450 linalool 8-methyl hydroxylase.
abstract: The cytochrome P-450 heme-thiolate monooxygenases that hydroxylate monoterpene hydrocarbon groups are effective models for the cytochrome P-450 family. We have purified and characterized the three proteins from a P-450-dependent linalool 8-methyl hydroxylase in Pseudomonas putida (incognita) strain PpG777. The proteins resemble the camphor 5-exohydroxylase components in chemical and physical properties; however, they show neither immunological cross-reactivity nor catalytic activity in heterogenous recombination. These two systems provide an excellent model to probe more deeply the heme-thiolate reaction center, molecular domains of substrate specificity, redox-pair interactions, and the regulation of the reaction cycle.
authors.affiliation: Department of Biochemistry, University of Illinois, Urbana 61801.
authors.forename: A J
authors.initials: AJ
authors.lastname: Ullah
authors.forename: R I
authors.initials: RI
authors.lastname: Murray
authors.forename: P K
authors.initials: PK
authors.lastname: Bhattacharyya
authors.forename: G C
authors.initials: GC
authors.lastname: Wagner
authors.forename: I C
authors.initials: IC
authors.lastname: Gunsalus
mesh_terms: D000080462:Acyclic Monoterpenes; D000596:Amino Acids / Q000032:analysis; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification / Q000378:metabolism*; D046911:Macromolecular Substances; D006899:Mixed Function Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D039821:Monoterpenes; D010088:Oxidoreductases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D013057:Spectrum Analysis; D013729:Terpenes / Q000378:metabolism
chemical_list: D000080462:Acyclic Monoterpenes; D000596:Amino Acids; D046911:Macromolecular Substances; D039821:Monoterpenes; D013729:Terpenes; D003577:Cytochrome P-450 Enzyme System; C018584:linalool; D006899:Mixed Function Oxygenases; D010088:Oxidoreductases; C059620:linalool 8-monooxygenase